Microtubule posttranslational modifications provide unique recognition patterns for associated proteins

ABSTRACT: Microtubules are key components of the eukaryotic cytoskeleton involved in vital functions in virtually every cell. Among the emerging molecular mechanisms to adapt microtubules to their diverse functions is the biochemical diversification of tubulin molecules by posttranslational modifications (PTMs) and differential gene expression, a concept known as the 'tubulin code'. A key question remains whether the tubulin code has the potential to selectively control microtubule interactions of different microtubule-associated proteins (MAPs) to act as a specific signalling system. To answer this question, we used a medium-throughput in vitro approach to screen 46 proteins for their binding preferences to microtubules with altered PTM or isotype composition. We demonstrate that subsets of these M

SUBMITTER: Arya Krishnan 

PROVIDER: S-SCDT-10_1038-S44318-026-00908-8 | biostudies-other |

REPOSITORIES: biostudies-other